Isolation and purification of chloroplastic spinach (<i>Spinacia oleracea</i>) sedoheptulose-1,7-bisphosphatase

Cadet, Frédéric; Meunier, Jean‐Claude; Ferté, Nathalie

doi:10.1042/bj2410071

Cited by 42 publications

(24 citation statements)

References 18 publications

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“…We could assign four proteins that already were reported as the target of the chloroplast Trx: Rubisco activase 45 kDa (20), GAPDH (14), sedoheptulose 1,7-bisphosphatase (16,37), and 2-Cys Prx (25). Additionally the known proteins, glutamine synthetase (GS) (monomer molecular mass 44 kDa), Rubisco activase (41 kDa), and Rubisco small subunit were obtained.…”

Section: Resultsmentioning

confidence: 99%

“…Four enzymes in the Calvin cycle-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (14), fructose 1,6-bisphosphatase (15), sedoheptulose 1,7-bisphosphatase (SBPase) (16), and phosphoribulokinase (17)-and CF 1 from thylakoid membranes (18) are reported as targets for Trx-f. NADP-dependent malate dehydrogenase was assigned as a target for Trx-m (4). However, the whole network involved in the redox cascade in chloroplasts is as yet not well known, although a lot of the enzyme activities are obviously regulated by light and the accompanying electron transport.…”

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confidence: 99%

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Comprehensive survey of proteins targeted by chloroplast thioredoxin

Motohashi

Kondoh

Stumpp

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

359

344

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Possible target proteins of chloroplast thioredoxin (Trx) have been investigated in the stroma lysate of spinach chloroplasts. For that purpose, we immobilized a mutant of m-type Trx in which an internal cysteine at the active site was substituted with serine, on cyanogen bromide-activated resin. By using this resin, the target proteins in chloroplast were efficiently acquired when they formed the mixed-disulfide intermediates with the immobilized Trxs. We could acquire Rubisco activase (45 kDa) and 2-Cys-type peroxiredoxin (Prx), which were recently identified as targets of chloroplast Trxs. Glyceraldehyde-3-phosphate dehydrogenase and sedoheputulose 1,7-bisphosphatase, well-known thiol enzymes in the Calvin cycle, also were recognized among the collected proteins, suggesting the method is applicable for our purpose. Furthermore, four proteins were identified from a homology search of the NH 2-terminal sequence of the acquired proteins: glutamine synthetase, a protein homologous to chloroplast cyclophilin, a homolog of Prx-Q, and the Rubisco small subunit. The Trx susceptibilities of the recombinant cyclophilin and Prx-Q of Arabidopsis thaliana were then examined. The method developed in the present study is thus applicable to investigate the various redox networks via Trxs and the related enzymes in the cell.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Comprehensive survey of proteins targeted by chloroplast thioredoxin

Motohashi

Kondoh

Stumpp

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

359

344

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“…While in photosynthetic bacteria, such as cyanobacteria, a single promiscuous enzyme carries out both reactions (36), in green plants, two separate enzymes catalyze the individual reactions. SBPases are homodimeric, comprising two identical subunits of 35 to 38 kDa, and are immunologically distinct from FBPase (37,38).…”

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confidence: 99%

Characterization of Fructose 1,6-Bisphosphatase and Sedoheptulose 1,7-Bisphosphatase from the Facultative Ribulose Monophosphate Cycle Methylotroph Bacillus methanolicus

Stolzenberger¹,

Lindner

Persicke

et al. 2013

J Bacteriol

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The genome of the facultative ribulose monophosphate (RuMP) cycle methylotroph Bacillus methanolicus encodes two bisphosphatases (GlpX), one on the chromosome (GlpX C ) and one on plasmid pBM19 (GlpX P ), which is required for methylotrophy. Both enzymes were purified from recombinant Escherichia coli and were shown to be active as fructose 1,6-bisphosphatases (FBPases). The FBPase-negative Corynebacterium glutamicum ⌬fbp mutant could be phenotypically complemented with glpX C and glpX P from B. methanolicus. GlpX P and GlpX C share similar functional properties, as they were found here to be active as homotetramers in vitro, activated by Mn 2؉ ions and inhibited by Li ؉ , but differed in terms of the kinetic parameters. GlpX C showed a much higher catalytic efficiency and a lower K m for fructose 1,6-bisphosphate (86.3 s ؊1 mM ؊1 and 14 ؎ 0.5 M, respectively) than GlpX P (8.8 s ؊1 mM ؊1 and 440 ؎ 7.6 M, respectively), indicating that GlpX C is the major FBPase of B. methanolicus. Both enzymes were tested for activity as sedoheptulose 1,7-bisphosphatase (SBPase), since a SBPase variant of the ribulose monophosphate cycle has been proposed for B. methanolicus. The substrate for the SBPase reaction, sedoheptulose 1,7-bisphosphate, could be synthesized in vitro by using both fructose 1,6-bisphosphate aldolase proteins from B. methanolicus. Evidence for activity as an SBPase could be obtained for GlpX P but not for GlpX C . Based on these in vitro data, GlpX P is a promiscuous SBPase/FBPase and might function in the RuMP cycle of B. methanolicus.

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“…This switch region consists of 37 amino acid residues (Pro 194 -Ile 230 in case of the spinach chloroplast enzyme) containing two cysteine residues, but its structure is unknown, and there are no data available on how reduction of the disulfide bond leads to activation of the enzyme. Such redox regulation is a common property of socalled thiol enzymes in the chloroplasts like glyceraldehyde-3-phosphate dehydrogenase (17), fructose-1,6-bisphosphatase (18), sedoheptulose-1,7-bisphosphatase (19), phosphoribulokinase (20), and NADP-malate dehydrogenase (21). The chloroplast thioredoxin, which is reduced by electron flow from photosystem, plays a main role in this regulation system (21).…”

mentioning

confidence: 99%

Redox Regulation of the Rotation of F1-ATP Synthase

Bald¹,

Noji²,

Yoshida³

et al. 2001

Journal of Biological Chemistry

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In F 1 -ATPase, the smallest known motor enzyme, unidirectional rotation of the central axis subunit ␥ is coupled to ATP hydrolysis. In the present study, we report the redox switching of the rotation of this enzyme. For this purpose, the switch region from the ␥ subunit of the redox-sensitive chloroplast F O F 1 -ATP synthase, which is located on the mitochondrial inner membranes, chloroplast thyalkoid membranes, and bacterial plasma membranes, synthesizes ATP, which is known as the universal energy "coin" in the cell, from ADP and phosphate at the expense of the proton gradient across the membranes (1). The water-soluble part of ATP synthase, the F 1 region, consists of five subunits with a composition of ␣ 3 ␤ 3 ␥ 1 ␦ 1 ⑀ 1 (2). The hydrophobic F O part is composed of a 1 b 2 c 10 -14 (3-5). The subcomplex of F 1 part, ␣ 3 ␤ 3 ␥, is the minimum complex that is capable of ATP hydrolysis (6). Rotation of the ␥ subunit in the ␣ 3 ␤ 3 hexagon was first postulated by P. D. Boyer and co-workers (8) from the analysis of the cooperative kinetics of F 1 -ATPase. A high resolution x-ray structure of a major part of the bovine heart mitochondrial F 1 (7) revealed an alternating hexagonal arrangement of the ␣ 3 ␤ 3 ring with the ␥ subunit as a central axis. Then the rotation of ␥ in the central cavity of ␣ 3 ␤ 3 was suggested by biochemical experiments (10), and finally, direct visualization of the rotation of an actin filament attached to the ␥ subunit of F 1 showed unequivocally that ␥ rotates unidirectionally during ATP hydrolysis (11)(12)(13)(14).The chloroplast ATP synthase has basically the same structure as those from other sources. However the enzyme activity of chloroplast ATP synthase (CF O CF 1 ) from higher plants is modulated in a unique way, reduction of a disulfide bridge in the ␥ subunit (15, 16). In the solubilized CF 1 part, the reduction of this disulfide bond, which is located in a switch region on ␥ unique to chloroplast ATP synthase, strongly enhances the ATP hydrolysis activity (ATPase activity). This switch region consists of 37 amino acid residues (Pro 194 -Ile 230 in case of the spinach chloroplast enzyme) containing two cysteine residues, but its structure is unknown, and there are no data available on how reduction of the disulfide bond leads to activation of the enzyme. Such redox regulation is a common property of socalled thiol enzymes in the chloroplasts like glyceraldehyde-3-phosphate dehydrogenase (17), fructose-1,6-bisphosphatase (18), sedoheptulose-1,7-bisphosphatase (19), phosphoribulokinase (20), and NADP-malate dehydrogenase (21). The chloroplast thioredoxin, which is reduced by electron flow from photosystem, plays a main role in this regulation system (21). However, to our knowledge there are no data available, neither for chloroplast enzymes nor for enzymes from other organelles, on whether regulation affects the reaction rate of a single enzyme molecule or influences the number of active enzyme molecules. To address this question, observation of the rotation of F 1 -ATPase is th...

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Isolation and purification of chloroplastic spinach (Spinacia oleracea) sedoheptulose-1,7-bisphosphatase

Cited by 42 publications

References 18 publications

Comprehensive survey of proteins targeted by chloroplast thioredoxin

Comprehensive survey of proteins targeted by chloroplast thioredoxin

Characterization of Fructose 1,6-Bisphosphatase and Sedoheptulose 1,7-Bisphosphatase from the Facultative Ribulose Monophosphate Cycle Methylotroph Bacillus methanolicus

Redox Regulation of the Rotation of F1-ATP Synthase

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